Chromatographic alignment of LC-MS and LC-MS/MS datasets by genetic algorithm feature extraction
نویسندگان
چکیده
منابع مشابه
A statistical method for chromatographic alignment of LC-MS data.
Integrated liquid-chromatography mass-spectrometry (LC-MS) is becoming a widely used approach for quantifying the protein composition of complex samples. The output of the LC-MS system measures the intensity of a peptide with a specific mass-charge ratio and retention time. In the last few years, this technology has been used to compare complex biological samples across multiple conditions. One...
متن کاملChromatographic alignment of ESI-LC-MS proteomics data sets by ordered bijective interpolated warping.
Mass spectrometry proteomics typically relies upon analyzing outcomes of single analyses; however, comparing raw data across multiple experiments should enhance both peptide/protein identification and quantitation. In the absence of convincing tandem MS identifications, comparing peptide quantities between experiments (or fractions) requires the chromatographic alignment of MS signals. An exten...
متن کاملAnnotation of LC-MS metabolomics datasets by the “metaMS” package
metaMS is designed to perform the analysis of LC-MS and GC-MSbased metabolomics assays. For LC-MS data, its major function runLC() is a wrapper around the functions and classes of xcms and CAMERA and it is designed to process a series of data files producing a peak table with the intensity of each feature an mz,rt couple in each one of the samples. The functions and classes of xcms and CAMERA a...
متن کاملAn Algorithm for Feature Finding in LC/MS Raw Data
Liquid chromatography coupled with mass spectrometry is an established method in shotgun proteomics. A key step in the data processing pipeline is to transform the raw data acquired by the mass spectrometer into a list of features. In this context, a feature is defined as the twodimensional integration with respect to retention time (RT) and mass-over-charge (m/z) of the eluting signal belongin...
متن کاملLC-MS and LC-MS/MS studies of incorporation of 34SO3 into glycosaminoglycan chains by sulfotransferases.
The specificities of glycosaminoglycan (GAG) modification enzymes, particularly sulfotransferases, and the locations and concentrations of these enzymes in the Golgi apparatus give rise to the mature GAG polysaccharides that bind protein ligands. We studied the substrate specificities of sulfotransferases with a stable isotopically labeled donor substrate, 3'-phosphoadenosine-5'-phosphosulfate....
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of the American Society for Mass Spectrometry
سال: 2007
ISSN: 1044-0305,1879-1123
DOI: 10.1016/j.jasms.2007.07.018